[The primary structure of hemoglobin from goldfish (Carassius auratus)]

Hoppe Seylers Z Physiol Chem. 1984 Jan;365(1):95-104. doi: 10.1515/bchm2.1984.365.1.95.
[Article in German]


The primary structures of the alpha- and beta-chains from goldfish hemoglobin are given. The globin chains were separated by gel filtration after air-oxidation of globin. After chemical and enzymatical cleavage of the chains, the peptides were isolated by gel filtration and ion exchange chromatography on Dowex. The fish-chains have one residue more than the human chains. The alpha-chain is acetylated at the amino-terminal residue and has no cysteine. Compared with the human chains there are 66 amino-acid differences in the alpha- and 72 in the beta-chains. The implication of these differences for the physiology of the hemoglobin molecule of goldfish is discussed.

Publication types

  • English Abstract

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chemical Phenomena
  • Chemistry
  • Chymotrypsin
  • Cyprinidae / blood*
  • Electrophoresis, Polyacrylamide Gel
  • Goldfish / blood*
  • Hemoglobins / isolation & purification*
  • Hydrolysis
  • Mass Spectrometry
  • Peptide Fragments / isolation & purification
  • Trypsin


  • Hemoglobins
  • Peptide Fragments
  • Chymotrypsin
  • Trypsin